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Literature summary for 3.1.3.11 extracted from

  • Fushinobu, S.; Nishimasu, H.; Hattori, D.; Song, H.J.; Wakagi, T.
    Structural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase (2011), Nature, 478, 538-541.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y229F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 1.1fold higher than the wild-type value, no fructose-bisphosphate aldolase activity Sulfurisphaera tokodaii
Y348F the kcat/Km-value of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) for D-fructose 1,6-bisphosphate is 3.5fold lower than the wild-type value, the kcat/Km-value for the fructose-bisphosphate aldolase reaction of the bifunctional enzyme (EC 3.1.3.11/EC 4.1.2.13) in the anabolic direction is 16fold lower than wild-type value Sulfurisphaera tokodaii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii
0.027
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
0.036
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii

Organism

Organism UniProt Comment Textmining
Sulfurisphaera tokodaii F9VMT6
-
-
Sulfurisphaera tokodaii 7 F9VMT6
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate + H2O the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii D-fructose 6-phosphate + phosphate
-
r
D-fructose 1,6-bisphosphate + H2O the bifunctional enzyme also shows activity of EC 4.1.2.13. The crystal structures of the enzyme in the two forms reveals that it achieves its bifunctionality by transforming its active-site architecture, through the toggle switch-like motions of the three mobile loop regions Sulfurisphaera tokodaii 7 D-fructose 6-phosphate + phosphate
-
r

Synonyms

Synonyms Comment Organism
FBP aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
FBPA/P bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
fructose-1,6-bisphosphate aldolase/phosphatase bifunctional enzyme EC 3.1.3.11/EC 4.1.2.13 Sulfurisphaera tokodaii
STK_03180 locus name. The bifunctional enzyme also shows activity of EC 4.1.2.13 Sulfurisphaera tokodaii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
48
-
assay at Sulfurisphaera tokodaii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.26
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
0.62
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
0.66
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
assay at Sulfurisphaera tokodaii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
7.2
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y348F Sulfurisphaera tokodaii
23
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, wild-type enzyme Sulfurisphaera tokodaii
25
-
D-fructose 1,6-bisphosphate pH 7.8, 48°C, mutant enzyme Y229F Sulfurisphaera tokodaii